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2015 - 2016

Chemistry Investigatory Project

MIDLAJ FAHEEM
XII a

ACKNOWLEGEMENT
I would like to express my immense gratitude
to my chemistry teacher Mr. Vinod Prabhu ,
for the help and guidance he provided for
completing the investigatory project.
I also thank my parents who gave their ideas and
inputs in making this Project. Most of all I thank
our school management, for providing us the
facilities and opportunity to do this project.
Lastly, I would like to thank my school mates who
have rendered and done this project along with me.
Their support made this project fruitful.

- MIDLAJ FAHEEM

BONAFIDE CERTIFICATE
This is to certify that Master Midlaj Faheem Bin
Mohammed has completed his project work entitled
Casein in Milk as a part of the paper of Chemistry,
under my guidance and supervision in the
department of Chemistry. To the best of my
knowledge, it is an original piece of his work. It is
worthy of consideration in partial fulfilment of the
requirement of CBSE, Delhi for the All India Senior
Secondary Examination in the subject Chemistry.
Name of guide:
Mr. Vinod Prabhu

School seal:

Principal:
Mr. Arogya Reddy

External Examiner:

Objective
To study the quantity of Casein
present in different brands of
milk.

Introduction
Milk is a complete diet as it contains
proteins, carbohydrates, fats, minerals, vitamins
and water. The average composition of milk from
different sources is given below:
BRAND
OF MILK

ENERGY

PROTEINS

FATS

CARBOHYDRAT
ES

AL MARAI

kJ/100 ml gm/100
ml
240
3.1

NADA

242

3.0

3.0

5.0

SAUDIA

243

3.2

3.2

5.1

(gm/100
ml)
3.1

(gm/100 ml)
4.7

Casein is the most predominant


phosphoprotein found in milk and cheese. When
coagulated with chymosin, casein is sometimes
called Paracasein. British terminology, on the
other hand, uses the term caseinogen for the
uncoagulated protein and casein for coagulated
protein. As it exists in milk, it is a salt of calcium.
Casein is not coagulated by heat. It is
precipitated by acids and by rennet enzymes, a
proteolytic enzyme typically obtained from the
stomachs of calves. The enzyme trypsin can
hydrolyze off a phosphate-containing peptone.

Casein consists of a fairly high number of


praline peptides, which do not interact. There are
also no disulphide bridges. As a result, it has
relatively little secondary structure or tertiary
structure. Because of this, it cannot denature. It is
relatively hydrophobic, making it poorly soluble in
water. It is found in milk as a suspension of
particles called casein micelles which show some
resemblance with surfactant-type micellae in a
sense that the hydrophilic parts reside at the
surface. The caseins in the micelles are held
together by calcium ions and hydrophobic
interactions. These micelles have negative charge
and on adding acid to milk the negative charges
are neutralized.

Ca

2+

- Caesinate + 2CH3COOH(aq) Casein+


(CH3COO)2Ca(aq)

The isoelectric point of casein is 4.7. The


purified protein is water insoluble. While it is also
insoluble in neutral salt solutions, it is readily
dispersible in dilute alkalis and in salt solutions
such as sodium oxalate and sodium acetate.

Applications:
In addition to being consumed in milk, casein
in used in the manufacture of adhesives, binders,
protective coatings, plastics (such as for knife
handles and knitting needles), fabrics, food
additives and many other products. It is commonly
used by bodybuilders as a slow-digestive source of
amino acids as opposed to the fast-digesting whey
protein, and also as an extremely high source of
glutamine (post workout). Another reason it is used
in bodybuilding, is because of its anti-catabolic
effect, meaning that casein consumption inhibits
protein breakdown in the body. Casein is frequently
found in otherwise nondairy cheese substitutes to
improve consistency especially when melted.

Aim
To study quantity of casein in different samples of
milk.

Theory
Milk contains 3 to 4% casein suspended in water
in the colloidal form. It is precipitated in a weakly
acidic medium.

Apparatus Required
Funnel, funnel stand , glass rod , filter paper,
weight box , test tubes, pestle and mortar.

Chemicals Required
(i) Different samples of milk.
(ii) Saturated ammonium sulphate solution.
(iii)

1 % acetic acid solution.

Procedure
1. Wash the beaker (250 ml) with the distilled water
and dry it.
2. Take 200 ml of buffalos milk in 200 ml
beaker and find its weight.
3. Add 20 ml saturated solution of ammonium
sulphate slowly with stirring. Fat and casein will
separate out as precipitate.
4. Filter the above solution and transfer the
precipitate in another beaker.
5. Treat the above precipitate with 30 ml distilled
water. Casein dissolves forming milky solution
whereas fat remains as such.
6. Warm the above contents of the beaker to 40 45C on a low flame. Now, add 1% acetic acid
solution drop wise with stirring when casein gets
precipitated.
7. Filter the precipitated casein and wash with
distilled water and dry it.
8. Find the weight of dry precipitate.

9. Repeat the whole experiment with different


samples of milk.

Observations
Volume of milk taken in each case
= 200 ml Weight of milk taken =
W g
Weight of Casein isolated = W g
Percentage of casein = Weight of Casein x 100
Weight of
milk

S.no. Brand of k Volume


of milk
mil
taken
(ml)
1.
Al Marai
200

Weigh Weight
t
of
of
milk
Casein
(W
(W g)
203.0
6.2
9

Percentage
of
casein
3.05%

2.

Nada

200

202.5
1

6.0

2.96%

3.

Saudia

200

203.0
6

6.4

3.15%

Result
Different Samples of milk contains different
percentage of casein.
Highest percentage of casein is present in Saudia
milk.

Precautions
1.

Handle apparatus and chemicals


carefully.
2. Add ammonium sulphate solution very
slowly.
3.
Stir milk while adding chemicals.
4. Do not disturb milk after adding
ammonium sulphate solution and wait
some time for fat and casein to
precipitate out.
5.
Take the amount readings carefully
with digital weighing machine only.

Bibliography
www.wikipedia.com
www.encyclopedia.co
m www.caesinepro.com
www.sciencejournals.
com www.icar.nic.in
www.zetascience.com
www.scribd.com

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